Search Results for: label/Geek Feminism

Post navigation

The four basic categories of molecules for building life are carbohydrates, lipids, proteins, and nucleic acids.

Carbohydrates serve many purposes, from energy to structure to chemical communication, as monomers or polymers.

Lipids, which are hydrophobic, also have different purposes, including energy storage, structure, and signaling.

Proteins, made of amino acids in up to four structural levels, are involved in just about every process of life.

The nucleic acids DNA and RNA consist of four nucleotide building blocks, and each has different purposes.

The longer version

Life is so diverse and unwieldy, it may surprise you to learn that we can break it down into four basic categories of molecules. Possibly even more implausible is the fact that two of these categories of large molecules themselves break down into a surprisingly small number of building blocks. The proteins that make up all of the living things on this planet and ensure their appropriate structure and smooth function consist of only 20 different kinds of building blocks. Nucleic acids, specifically DNA, are even more basic: only four different kinds of molecules provide the materials to build the countless different genetic codes that translate into all the different walking, swimming, crawling, oozing, and/or photosynthesizing organisms that populate the third rock from the Sun.

Big Molecules with Small Building Blocks

The functional groups, assembled into building blocks on backbones of carbon atoms, can be bonded together to yield large molecules that we classify into four basic categories. These molecules, in many different permutations, are the basis for the diversity that we see among living things. They can consist of thousands of atoms, but only a handful of different kinds of atoms form them. It’s like building apartment buildings using a small selection of different materials: bricks, mortar, iron, glass, and wood. Arranged in different ways, these few materials can yield a huge variety of structures.

We encountered functional groups and the SPHONC in Chapter 3. These components form the four categories of molecules of life. These Big Four biological molecules are carbohydrates, lipids, proteins, and nucleic acids. They can have many roles, from giving an organism structure to being involved in one of the millions of processes of living. Let’s meet each category individually and discover the basic roles of each in the structure and function of life.

Carbohydrates

You have met carbohydrates before, whether you know it or not. We refer to them casually as “sugars,” molecules made of carbon, hydrogen, and oxygen. A sugar molecule has a carbon backbone, usually five or six carbons in the ones we’ll discuss here, but it can be as few as three. Sugar molecules can link together in pairs or in chains or branching “trees,” either for structure or energy storage.

When you look on a nutrition label, you’ll see reference to “sugars.” That term includes carbohydrates that provide energy, which we get from breaking the chemical bonds in a sugar called glucose. The “sugars” on a nutrition label also include those that give structure to a plant, which we call fiber. Both are important nutrients for people.

Sugars serve many purposes. They give crunch to the cell walls of a plant or the exoskeleton of a beetle and chemical energy to the marathon runner. When attached to other molecules, like proteins or fats, they aid in communication between cells. But before we get any further into their uses, let’s talk structure.

The sugars we encounter most in basic biology have their five or six carbons linked together in a ring. There’s no need to dive deep into organic chemistry, but there are a couple of essential things to know to interpret the standard representations of these molecules.

Check out the sugars depicted in the figure. The top-left molecule, glucose, has six carbons, which have been numbered. The sugar to its right is the same glucose, with all but one “C” removed. The other five carbons are still there but are inferred using the conventions of organic chemistry: Anywhere there is a corner, there’s a carbon unless otherwise indicated. It might be a good exercise for you to add in a “C” over each corner so that you gain a good understanding of this convention. You should end up adding in five carbon symbols; the sixth is already given because that is conventionally included when it occurs outside of the ring.

On the left is a glucose with all of its carbons indicated. They’re also numbered, which is important to understand now for information that comes later. On the right is the same molecule, glucose, without the carbons indicated (except for the sixth one). Wherever there is a corner, there is a carbon, unless otherwise indicated (as with the oxygen). On the bottom left is ribose, the sugar found in RNA. The sugar on the bottom right is deoxyribose. Note that at carbon 2 (*), the ribose and deoxyribose differ by a single oxygen.

The lower left sugar in the figure is a ribose. In this depiction, the carbons, except the one outside of the ring, have not been drawn in, and they are not numbered. This is the standard way sugars are presented in texts. Can you tell how many carbons there are in this sugar? Count the corners and don’t forget the one that’s already indicated!

If you said “five,” you are right. Ribose is a pentose (pent = five) and happens to be the sugar present in ribonucleic acid, or RNA. Think to yourself what the sugar might be in deoxyribonucleic acid, or DNA. If you thought, deoxyribose, you’d be right.

The fourth sugar given in the figure is a deoxyribose. In organic chemistry, it’s not enough to know that corners indicate carbons. Each carbon also has a specific number, which becomes important in discussions of nucleic acids. Luckily, we get to keep our carbon counting pretty simple in basic biology. To count carbons, you start with the carbon to the right of the non-carbon corner of the molecule. The deoxyribose or ribose always looks to me like a little cupcake with a cherry on top. The “cherry” is an oxygen. To the right of that oxygen, we start counting carbons, so that corner to the right of the “cherry” is the first carbon. Now, keep counting. Here’s a little test: What is hanging down from carbon 2 of the deoxyribose?

If you said a hydrogen (H), you are right! Now, compare the deoxyribose to the ribose. Do you see the difference in what hangs off of the carbon 2 of each sugar? You’ll see that the carbon 2 of ribose has an –OH, rather than an H. The reason the deoxyribose is called that is because the O on the second carbon of the ribose has been removed, leaving a “deoxyed” ribose. This tiny distinction between the sugars used in DNA and RNA is significant enough in biology that we use it to distinguish the two nucleic acids.

In fact, these subtle differences in sugars mean big differences for many biological molecules. Below, you’ll find a couple of ways that apparently small changes in a sugar molecule can mean big changes in what it does. These little changes make the difference between a delicious sugar cookie and the crunchy exoskeleton of a dung beetle.

Sugar and Fuel

A marathon runner keeps fuel on hand in the form of “carbs,” or sugars. These fuels provide the marathoner’s straining body with the energy it needs to keep the muscles pumping. When we take in sugar like this, it often comes in the form of glucose molecules attached together in a polymer called starch. We are especially equipped to start breaking off individual glucose molecules the minute we start chewing on a starch.

Double X Extra: A monomer is a building block (mono = one) and a polymer is a chain of monomers. With a few dozen monomers or building blocks, we get millions of different polymers. That may sound nutty until you think of the infinity of values that can be built using only the numbers 0 through 9 as building blocks or the intricate programming that is done using only a binary code of zeros and ones in different combinations.

Our bodies then can rapidly take the single molecules, or monomers, into cells and crack open the chemical bonds to transform the energy for use. The bonds of a sugar are packed with chemical energy that we capture to build a different kind of energy-containing molecule that our muscles access easily. Most species rely on this process of capturing energy from sugars and transforming it for specific purposes.

Polysaccharides: Fuel and Form

Plants use the Sun’s energy to make their own glucose, and starch is actually a plant’s way of storing up that sugar. Potatoes, for example, are quite good at packing away tons of glucose molecules and are known to dieticians as a “starchy” vegetable. The glucose molecules in starch are packed fairly closely together. A string of sugar molecules bonded together through dehydration synthesis, as they are in starch, is a polymer called a polysaccharide (poly = many; saccharide = sugar). When the monomers of the polysaccharide are released, as when our bodies break them up, the reaction that releases them is called hydrolysis.

Double X Extra: The specific reaction that hooks one monomer to another in a covalent bond is called dehydration synthesis because in making the bond–synthesizing the larger molecule–a molecule of water is removed (dehydration). The reverse is hydrolysis (hydro = water; lysis = breaking), which breaks the covalent bond by the addition of a molecule of water.

Although plants make their own glucose and animals acquire it by eating the plants, animals can also package away the glucose they eat for later use. Animals, including humans, store glucose in a polysaccharide called glycogen, which is more branched than starch. In us, we build this energy reserve primarily in the liver and access it when our glucose levels drop.

Whether starch or glycogen, the glucose molecules that are stored are bonded together so that all of the molecules are oriented the same way. If you view the sixth carbon of the glucose to be a “carbon flag,” you’ll see in the figure that all of the glucose molecules in starch are oriented with their carbon flags on the upper left.

The orientation of monomers of glucose in polysaccharides can make a big difference in the use of the polymer. The glucoses in the molecule on the top are all oriented “up” and form starch. The glucoses in the molecule on the bottom alternate orientation to form cellulose, which is quite different in its function from starch.

Storing up sugars for fuel and using them as fuel isn’t the end of the uses of sugar. In fact, sugars serve as structural molecules in a huge variety of organisms, including fungi, bacteria, plants, and insects.

The primary structural role of a sugar is as a component of the cell wall, giving the organism support against gravity. In plants, the familiar old glucose molecule serves as one building block of the plant cell wall, but with a catch: The molecules are oriented in an alternating up-down fashion. The resulting structural sugar is called cellulose.

That simple difference in orientation means the difference between a polysaccharide as fuel for us and a polysaccharide as structure. Insects take it step further with the polysaccharide that makes up their exoskeleton, or outer shell. Once again, the building block is glucose, arranged as it is in cellulose, in an alternating conformation. But in insects, each glucose has a little extra added on, a chemical group called an N-acetyl group. This addition of a single functional group alters the use of cellulose and turns it into a structural molecule that gives bugs that special crunchy sound when you accidentally…ahem…step on them.

These variations on the simple theme of a basic carbon-ring-as-building-block occur again and again in biological systems. In addition to serving roles in structure and as fuel, sugars also play a role in function. The attachment of subtly different sugar molecules to a protein or a lipid is one way cells communicate chemically with one another in refined, regulated interactions. It’s as though the cells talk with each other using a specialized, sugar-based vocabulary. Typically, cells display these sugary messages to the outside world, making them available to other cells that can recognize the molecular language.

Lipids: The Fatty Trifecta

Starch makes for good, accessible fuel, something that we immediately attack chemically and break up for quick energy. But fats are energy that we are supposed to bank away for a good long time and break out in times of deprivation. Like sugars, fats serve several purposes, including as a dense source of energy and as a universal structural component of cell membranes everywhere.

Fats: the Good, the Bad, the Neutral

Turn again to a nutrition label, and you’ll see a few references to fats, also known as lipids. (Fats are slightly less confusing that sugars in that they have only two names.) The label may break down fats into categories, including trans fats, saturated fats, unsaturated fats, and cholesterol. You may have learned that trans fats are “bad” and that there is good cholesterol and bad cholesterol, but what does it all mean?

Let’s start with what we mean when we say saturated fat. The question is, saturated with what? There is a specific kind of dietary fat call the triglyceride. As its name implies, it has a structural motif in which something is repeated three times. That something is a chain of carbons and hydrogens, hanging off in triplicate from a head made of glycerol, as the figure shows. Those three carbon-hydrogen chains, or fatty acids, are the “tri” in a triglyceride. Chains like this can be many carbons long.

Double X Extra: We call a fatty acid a fatty acid because it’s got a carboxylic acid attached to a fatty tail. A triglyceride consists of three of these fatty acids attached to a molecule called glycerol. Our dietary fat primarily consists of these triglycerides.

Triglycerides come in several forms. You may recall that carbon can form several different kinds of bonds, including single bonds, as with hydrogen, and double bonds, as with itself. A chain of carbon and hydrogens can have every single available carbon bond taken by a hydrogen in single covalent bond. This scenario of hydrogen saturation yields a saturated fat. The fat is saturated to its fullest with every covalent bond taken by hydrogens single bonded to the carbons.

Saturated fats have predictable characteristics. They lie flat easily and stick to each other, meaning that at room temperature, they form a dense solid. You will realize this if you find a little bit of fat on you to pinch. Does it feel pretty solid? That’s because animal fat is saturated fat. The fat on a steak is also solid at room temperature, and in fact, it takes a pretty high heat to loosen it up enough to become liquid. Animals are not the only organisms that produce saturated fat–avocados and coconuts also are known for their saturated fat content.

The top graphic above depicts a triglyceride with the glycerol, acid, and three hydrocarbon tails. The tails of this saturated fat, with every possible hydrogen space occupied, lie comparatively flat on one another, and this kind of fat is solid at room temperature. The fat on the bottom, however, is unsaturated, with bends or kinks wherever two carbons have double bonded, booting a couple of hydrogens and making this fat unsaturated, or lacking some hydrogens. Because of the space between the bumps, this fat is probably not solid at room temperature, but liquid.

You can probably now guess what an unsaturated fat is–one that has one or more hydrogens missing. Instead of single bonding with hydrogens at every available space, two or more carbons in an unsaturated fat chain will form a double bond with carbon, leaving no space for a hydrogen. Because some carbons in the chain share two pairs of electrons, they physically draw closer to one another than they do in a single bond. This tighter bonding result in a “kink” in the fatty acid chain.

In a fat with these kinks, the three fatty acids don’t lie as densely packed with each other as they do in a saturated fat. The kinks leave spaces between them. Thus, unsaturated fats are less dense than saturated fats and often will be liquid at room temperature. A good example of a liquid unsaturated fat at room temperature is canola oil.

A few decades ago, food scientists discovered that unsaturated fats could be resaturated or hydrogenated to behave more like saturated fats and have a longer shelf life. The process of hydrogenation–adding in hydrogens–yields trans fat. This kind of processed fat is now frowned upon and is being removed from many foods because of its associations with adverse health effects. If you check a food label and it lists among the ingredients “partially hydrogenated” oils, that can mean that the food contains trans fat.

Double X Extra: A triglyceride can have up to three different fatty acids attached to it. Canola oil, for example, consists primarily of oleic acid, linoleic acid, and linolenic acid, all of which are unsaturated fatty acids with 18 carbons in their chains.

Why do we take in fat anyway? Fat is a necessary nutrient for everything from our nervous systems to our circulatory health. It also, under appropriate conditions, is an excellent way to store up densely packaged energy for the times when stores are running low. We really can’t live very well without it.

Phospholipids: An Abundant Fat

You may have heard that oil and water don’t mix, and indeed, it is something you can observe for yourself. Drop a pat of butter–pure saturated fat–into a bowl of water and watch it just sit there. Even if you try mixing it with a spoon, it will just sit there. Now, drop a spoon of salt into the water and stir it a bit. The salt seems to vanish. You’ve just illustrated the difference between a water-fearing (hydrophobic) and a water-loving (hydrophilic) substance.

Generally speaking, compounds that have an unequal sharing of electrons (like ions or anything with a covalent bond between oxygen and hydrogen or nitrogen and hydrogen) will be hydrophilic. The reason is that a charge or an unequal electron sharing gives the molecule polarity that allows it to interact with water through hydrogen bonds. A fat, however, consists largely of hydrogen and carbon in those long chains. Carbon and hydrogen have roughly equivalent electronegativities, and their electron-sharing relationship is relatively nonpolar. Fat, lacking in polarity, doesn’t interact with water. As the butter demonstrated, it just sits there.

There is one exception to that little maxim about fat and water, and that exception is the phospholipid. This lipid has a special structure that makes it just right for the job it does: forming the membranes of cells. A phospholipid consists of a polar phosphate head–P and O don’t share equally–and a couple of nonpolar hydrocarbon tails, as the figure shows. If you look at the figure, you’ll see that one of the two tails has a little kick in it, thanks to a double bond between the two carbons there.

Phospholipids form a double layer and are the major structural components of cell membranes. Their bend, or kick, in one of the hydrocarbon tails helps ensure fluidity of the cell membrane. The molecules are bipolar, with hydrophilic heads for interacting with the internal and external watery environments of the cell and hydrophobic tails that help cell membranes behave as general security guards.

The kick and the bipolar (hydrophobic and hydrophilic) nature of the phospholipid make it the perfect molecule for building a cell membrane. A cell needs a watery outside to survive. It also needs a watery inside to survive. Thus, it must face the inside and outside worlds with something that interacts well with water. But it also must protect itself against unwanted intruders, providing a barrier that keeps unwanted things out and keeps necessary molecules in.

Phospholipids achieve it all. They assemble into a double layer around a cell but orient to allow interaction with the watery external and internal environments. On the layer facing the inside of the cell, the phospholipids orient their polar, hydrophilic heads to the watery inner environment and their tails away from it. On the layer to the outside of the cell, they do the same.

As the figure shows, the result is a double layer of phospholipids with each layer facing a polar, hydrophilic head to the watery environments. The tails of each layer face one another. They form a hydrophobic, fatty moat around a cell that serves as a general gatekeeper, much in the way that your skin does for you. Charged particles cannot simply slip across this fatty moat because they can’t interact with it. And to keep the fat fluid, one tail of each phospholipid has that little kick, giving the cell membrane a fluid, liquidy flow and keeping it from being solid and unforgiving at temperatures in which cells thrive.

Steroids: Here to Pump You Up?

Our final molecule in the lipid fatty trifecta is cholesterol. As you may have heard, there are a few different kinds of cholesterol, some of which we consider to be “good” and some of which is “bad.” The good cholesterol, high-density lipoprotein, or HDL, in part helps us out because it removes the bad cholesterol, low-density lipoprotein or LDL, from our blood. The presence of LDL is associated with inflammation of the lining of the blood vessels, which can lead to a variety of health problems.

But cholesterol has some other reasons for existing. One of its roles is in the maintenance of cell membrane fluidity. Cholesterol is inserted throughout the lipid bilayer and serves as a block to the fatty tails that might otherwise stick together and become a bit too solid.

Cholesterol’s other starring role as a lipid is as the starting molecule for a class of hormones we called steroids or steroid hormones. With a few snips here and additions there, cholesterol can be changed into the steroid hormones progesterone, testosterone, or estrogen. These molecules look quite similar, but they play very different roles in organisms. Testosterone, for example, generally masculinizes vertebrates (animals with backbones), while progesterone and estrogen play a role in regulating the ovulatory cycle.

Double X Extra: A hormone is a blood-borne signaling molecule. It can be lipid based, like testosterone, or short protein, like insulin.

Proteins

As you progress through learning biology, one thing will become more and more clear: Most cells function primarily as protein factories. It may surprise you to learn that proteins, which we often talk about in terms of food intake, are the fundamental molecule of many of life’s processes. Enzymes, for example, form a single broad category of proteins, but there are millions of them, each one governing a small step in the molecular pathways that are required for living.

Levels of Structure

Amino acids are the building blocks of proteins. A few amino acids strung together is called a peptide, while many many peptides linked together form a polypeptide. When many amino acids strung together interact with each other to form a properly folded molecule, we call that molecule a protein.

For a string of amino acids to ultimately fold up into an active protein, they must first be assembled in the correct order. The code for their assembly lies in the DNA, but once that code has been read and the amino acid chain built, we call that simple, unfolded chain the primary structure of the protein.

This chain can consist of hundreds of amino acids that interact all along the sequence. Some amino acids are hydrophobic and some are hydrophilic. In this context, like interacts best with like, so the hydrophobic amino acids will interact with one another, and the hydrophilic amino acids will interact together. As these contacts occur along the string of molecules, different conformations will arise in different parts of the chain. We call these different conformations along the amino acid chain the protein’s secondary structure.

Once those interactions have occurred, the protein can fold into its final, or tertiary structure and be ready to serve as an active participant in cellular processes. To achieve the tertiary structure, the amino acid chain’s secondary interactions must usually be ongoing, and the pH, temperature, and salt balance must be just right to facilitate the folding. This tertiary folding takes place through interactions of the secondary structures along the different parts of the amino acid chain.

The final product is a properly folded protein. If we could see it with the naked eye, it might look a lot like a wadded up string of pearls, but that “wadded up” look is misleading. Protein folding is a carefully regulated process that is determined at its core by the amino acids in the chain: their hydrophobicity and hydrophilicity and how they interact together.

In many instances, however, a complete protein consists of more than one amino acid chain, and the complete protein has two or more interacting strings of amino acids. A good example is hemoglobin in red blood cells. Its job is to grab oxygen and deliver it to the body’s tissues. A complete hemoglobin protein consists of four separate amino acid chains all properly folded into their tertiary structures and interacting as a single unit. In cases like this involving two or more interacting amino acid chains, we say that the final protein has a quaternary structure. Some proteins can consist of as many as a dozen interacting chains, behaving as a single protein unit.

A Plethora of Purposes

What does a protein do? Let us count the ways. Really, that’s almost impossible because proteins do just about everything. Some of them tag things. Some of them destroy things. Some of them protect. Some mark cells as “self.” Some serve as structural materials, while others are highways or motors. They aid in communication, they operate as signaling molecules, they transfer molecules and cut them up, they interact with each other in complex, interrelated pathways to build things up and break things down. They regulate genes and package DNA, and they regulate and package each other.

As described above, proteins are the final folded arrangement of a string of amino acids. One way we obtain these building blocks for the millions of proteins our bodies make is through our diet. You may hear about foods that are high in protein or people eating high-protein diets to build muscle. When we take in those proteins, we can break them apart and use the amino acids that make them up to build proteins of our own.

Nucleic Acids

How does a cell know which proteins to make? It has a code for building them, one that is especially guarded in a cellular vault in our cells called the nucleus. This code is deoxyribonucleic acid, or DNA. The cell makes a copy of this code and send it out to specialized structures that read it and build proteins based on what they read. As with any code, a typo–a mutation–can result in a message that doesn’t make as much sense. When the code gets changed, sometimes, the protein that the cell builds using that code will be changed, too.

Biohazard!The names associated with nucleic acids can be confusing because they all start with nucle-. It may seem obvious or easy now, but a brain freeze on a test could mix you up. You need to fix in your mind that the shorter term (10 letters, four syllables), nucleotide, refers to the smaller molecule, the three-part building block. The longer term (12 characters, including the space, and five syllables), nucleic acid, which is inherent in the names DNA and RNA, designates the big, long molecule.

DNA vs. RNA: A Matter of Structure

DNA and its nucleic acid cousin, ribonucleic acid, or RNA, are both made of the same kinds of building blocks. These building blocks are called nucleotides. Each nucleotide consists of three parts: a sugar (ribose for RNA and deoxyribose for DNA), a phosphate, and a nitrogenous base. In DNA, every nucleotide has identical sugars and phosphates, and in RNA, the sugar and phosphate are also the same for every nucleotide.

So what’s different? The nitrogenous bases. DNA has a set of four to use as its coding alphabet. These are the purines, adenine and guanine, and the pyrimidines, thymine and cytosine. The nucleotides are abbreviated by their initial letters as A, G, T, and C. From variations in the arrangement and number of these four molecules, all of the diversity of life arises. Just four different types of the nucleotide building blocks, and we have you, bacteria, wombats, and blue whales.

RNA is also basic at its core, consisting of only four different nucleotides. In fact, it uses three of the same nitrogenous bases as DNA–A, G, and C–but it substitutes a base called uracil (U) where DNA uses thymine. Uracil is a pyrimidine.

DNA vs. RNA: Function Wars

An interesting thing about the nitrogenous bases of the nucleotides is that they pair with each other, using hydrogen bonds, in a predictable way. An adenine will almost always bond with a thymine in DNA or a uracil in RNA, and cytosine and guanine will almost always bond with each other. This pairing capacity allows the cell to use a sequence of DNA and build either a new DNA sequence, using the old one as a template, or build an RNA sequence to make a copy of the DNA.

These two different uses of A-T/U and C-G base pairing serve two different purposes. DNA is copied into DNA usually when a cell is preparing to divide and needs two complete sets of DNA for the new cells. DNA is copied into RNA when the cell needs to send the code out of the vault so proteins can be built. The DNA stays safely where it belongs.

RNA is really a nucleic acid jack-of-all-trades. It not only serves as the copy of the DNA but also is the main component of the two types of cellular workers that read that copy and build proteins from it. At one point in this process, the three types of RNA come together in protein assembly to make sure the job is done right.

One of the goals of Double X Science is to raise the profile of women in science. When others are doing this exact same things, we like to let our readers know. Here’s a few recent efforts to expand the public’s knowledge of women scientists:

The Royal Society recently had a wikipedia push for writers to start new and expand the pages of women in science. Having visited wikipedia for writing the Notable Women in Science series, I can say that the number of pages created has definitely expanded and certainly there is much more information provided on a number of women. But there are still gaps. Look for more from Double X Science on this topic in the future.

A group in the UK is making a calendar “to showcase real women doing great science.” Learn more about ScienceGRRL by visiting their website and following thier social media. The images being used in the calendar look to be scenic or portrait-style.

SpotOn provides some tools for the female scientist to promote herself and also provides links that those interested in science might be interested in following, such as twitter lists of women in science.

When researching this post, I found several sites trying to promote women in science. This site provides resources as well as 4000 years of women in science. In addition, they link to many associations dedicated to helping women in science. Geek Feminism has Wednesday Geek Woman posts every Wednesday highlighting women in STEM. The RAISE project has an on-going blog about the issues facing women in science.

Please comment: What is your favorite site working to raise the profile of women in science and why?

These views are the opinion of the author and do not necessarily reflect or disagree with those of the DXS editorial team.

With the holidays fast approaching, the Double X Science team has come up with a great list of science-themed gifts to help you in your quest for the perfect present. Not only are these gifts thoughtful, they are full of thought. So go forth and spread some nerd love this year!

Apparel

I Love Science T-shirt, Amazon, $19.99 Let your loved ones tell the world around them that they are into science with this cool take on a T-shirt. I doubt that any of the Kardashians will be wearing this one.

The way we work by David Macaulay, Amazon, $23.10Recommended for ages 5 and above, this book elegantly demonstrates how and why our bodies function the way they do, from digestion, to respiration, to reproduction, all from the perspective of an engineer and illustrator.

Here Comes Science by They Might Be Giants, Amazon, $8.99This is a seriously wonderful music/DVD combo that uses catchy tunes and big voices to turn science into singable fun! My personal favorite is “Electric Car.” Here is a video form this collection about why the sun shines (my kids know every word):

Hometown Puzzle, National Geographic, $39.95Forget those generic puzzles found on the shelves of cookie-cutter toy stores, this highly personalized jigsaw will tickle the fancy of puzzle-lovers anywhere. I’m probably going to get this for my mom. NOTE: You need to order this by 12/13 if you want it by 12/25.

DNA Gel Travel Mug, Cafe Press, $24.50What’s in your cup is not nearly as cool as what’s on your cup! I’ve always said that DNA is beautiful, and with this mug, everyone will be able to see it. I’d venture to say that it would be a great conversation piece as well.

Liz Neeley is the assistant director at COMPASS where she helps develop and lead the communications trainings for scientists, and specializes in the social media and multimedia components of their workshops and outreach efforts. Before joining COMPASS, Liz studied the evolution and visual systems of tropical reef fishes at Boston University. After grad school, she helped communities and researchers in Fiji and Papua New Guinea connect their knowledge of local coral reefs ecosystems to the media. She also dabbled in international science policy while working on trade in deep-sea corals. Liz is currently based in Seattle, at the University of Washington. You can find Liz on Twitter (@LizNeeley) and on Google+. Also check our her passion projects, ScienceOnline Seattle and her SciLingual hangout series.

DXS: First, can you give us a quick overview of what your scientific background is and your current connection to science?

I was one of those kids who knew from a really young age what they wanted to be, and that was a fish biologist. Sea turtles, dolphins – no way – I wanted to study fish. My mom actually found an old picture I drew when I was in third grade about what I wanted to be when I grew up: it was me in a lab coat, holding a clipboard, and tanks of aquaria behind me.

You combine this with the fact that I am also a really stubborn person, and I just wanted to do science straight through all my schooling. Not just the coursework either – I did an NSF young scholars program in high school, was the captain of the engineering team, and, of course, was a mathlete.

I did my undergraduate work in marine biology at the University of Maryland. I did three years of research there on oyster reef restoration, and then went straight into my PhD at Boston University, where I studied the evolution of color patterns and visual systems in wrasses and parrotfish.

I actually did not finish my PhD. Life sort of knocked me sideways, and instead of finishing my PhD, I ended up taking a masters, and then going into the non-profit world. At first, I mostly worked on coral conservation in Fiji and Papua New Guinea, and I did a big project on deep sea corals.

After I left grad school, I started a 20-hour per week internship at an NGO called SeaWeb. Vikki Spruill, who was the founder and president, has killer instincts and a passion for women’s high fashion that I share. She had noticed coral jewelry coming down the runway in Milan, Paris, and NY. People just didn’t have any idea that these pieces of jewelry were actually animals, much less that they were deep sea corals.

So we launched a campaign called “Too Precious to Wear,” which partnered with high-end fashion and luxury designer to create alternatives to these deep sea corals – celebrating coral but not actually using it. The Tiffany & Co. Foundation was our major partner, and we got to throw a breakfast at Tiffany’s that brought in fashion editors from Mademoiselle and Vogue.

Everyone always dismisses women’s fashions as shallow and meaningless, but this ended up being this huge lever that got a lot of attention for deep sea coral conservation, and my piece was the science that pinned it all together. I got a taste of the international policy component of that as well, and headed to the Netherlands for CITES (the Convention on International Trade in Endangered Species) as part of the work. I knew the science, but certainly helped that I knew how to pronounce the names of the designers too – opportunities like that to bridge cultures that seem foreign to each other are tremendously powerful.

I currently work at COMPASS, which is an organization that works at the intersection of science, policy, and communication/media. Our tagline is “helping scientists find their voices and bringing science into the conversation.” For my part, this means, I teach science communications trainings around the country, helping researchers understand how social media works, how reporters find their stories, and how to overcome some of the obstacles that scientists often put in their own way when they talk about their work.

What I love about this work so much is that it keeps me in the science community – around people who are pursuing tough questions. That is how my brain works, it is how my soul works, and I want to be a part of it. The power of this for me is to be able to take in all of this knowledge that is generated by these scientists and help connect it to the broader world. I feel like this is the best contribution I can make.

DXS: What ways do you express yourself creatively that may not have a single thing to do with science?

I am a pretty artistic person – or at least I think of myself as a pretty artistic person! My creative outlets usually involve some kind of graphic design. I am always giving presentations for my work, and I constantly ask “what do my slides look like, and am I telling a good story?” I so lucky that I get to spend a lot of time thinking about imagery, visual storytelling, and how people react to art or data visualization.

I also paint and draw (though I wouldn’t really share those) and I cook. I am actually doing a bread baking experiment this year where I am trying out a different type of bread recipe every weekend.

It can be really funny because sometimes, if it has been a really stressful week, I will look for a recipe that really needs to be punched down or kneaded for a long time. It’s a good workout too! And then we have this amazing bread every weekend. It is all about the aesthetics for me – I host dinner parties, bake, have a great garden – all of that is sort of my own creative outlet.

Some experimental results from Liz’s bread project.

DXS: What is your favorite bread?

The delicious baguette

LN: Oh, the baguette. I made my own for the first time last weekend and it was really fantastic! I realize that baking is one of these things that, if you want to do it properly, you have to be very precise. You should weigh the ingredients. But I’m precise in the rest of my life. When it is the weekend and I am having fun, I kind of love it when the flour is just flying everywhere. As a result, my loaves are a little bit mutated, or just not quite right, but they are delicious! Some of my other favorites also includes a great focaccia (the recipe for it is below!).

DXS: Do you find that your scientific background informs your creativity, even though what you do may not specifically be scientific?

Yes, absolutely. It’s funny because when you asked the question about my creative outlets that have nothing to do with science, it was not entirely easy to answer. You know, science is who I am – it permeates everything I do. When I am baking the bread, I am thinking about the yeast and fermentation. When I am painting, I am thinking about color theory and visual perception – after all that would have been what my PhD was in!

Speaking of color theory, Joanne Manaster recently shared a “how good is your color vision?” quiz. I took that test immediately to see how I would do. That lead me on this interesting exploration around the literature, and I read one theory that Van Gogh might have had a certain type of color blindness. I love this question of how our brains interact with the world. In animal behavior the concept is called “umwelt” – each species has a unique sensory experience of the environment. I like to think about how that applies to individual people to a smaller degree.

I think about this all the time – science, creativity, art, aesthetics – it is all one beautiful and amazing thing to me.

DXS: Have you encountered situations in which your expression of yourself outside the bounds of science has led to people viewing you differently–either more positively or more negatively?

I accept the fact that, especially when it comes to strangers, we make up stories based on what we see – clothes, hair, etc. I know that this happens to me as well. When we talk about femininity, it’s no secret that I am a girly girl. I wear makeup and heels. That’s how I feel most like myself, how I feel best. I know that this doesn’t sit well with everybody, but that’s ok. I like to think that I hold my own. Give me enough time to speak my piece and I can back it up. I’ve got an interesting career, I am a geek, and it is not hard for me to connect with people once we start talking.

In science we say that we don’t have a dress code, but the reality is that we do. Maybe it’s unspoken, and sure it is not the same as you see in the business world, but when you look different from how everyone else looks, people do want comment on it. I don’t feel like it is particularly negative in my case, and I feel that it doesn’t impede me. What is most exciting is that it often opens up conversation – mostly with other women who say “oh I really like your dress, I’ve been wearing more dresses lately!”

When I was an undergrad, I was kind of oblivious to the whole dress code thing. One day, when I was in the lab, I was wearing this pink, strappy sundress, tied up the back, and these stupid platform sandals that were really tall (clearly not appropriate lab gear). I was scrubbing out this 100-gallon oyster tank and my advisor happened to walk by and he sees me doing this. I remember freezing – all of the sudden I was afraid he was going to mock me or lecture me, but he just said, “Oh, Liz… Keep on.”

My graduate advisor was the same way – he acknowledged who I am and didn’t bother about how I dress. We didn’t avoid the topic. It just wasn’t an issue. I hope that other women can have that same experience. It doesn’t matter if you are a tomboy or a girly-girl. I don’t care – I am not judging you. You don’t have to look like me because I am in a dress.

This is why I love this #IAmSciencememe, and the whole “be yourself” mentality. And that is what I am going to do. I’ve decided to be myself. I accept the fact that not everyone will like the look of me. But, I think that we will eventually get to the point where we understand that science can be presented in lots of different ways.

DXS: Have you found that your non-science expression of creativity/activity/etc. has in any way informed your understanding of science or how you may talk about it or present it to others?

For me, my job with COMPASS really is sitting at this nexus of asking how we share science with people who aren’t intrinsically fascinated by it or connected to it. This is very much a ripe field for thinking about creative expression. Mostly, we come at it in terms of verbal presentations, storytelling and written materials, but then I specialize in the social media and multimedia components. I am always thinking about everything I am reading and seeing – news, art, music, fiction – and how we can apply what resonates with others in these non-science realms. It is very much a two-way thing; my science informs my creativity and my creativity informs my science. That makes it really fulfilling and exciting for me.

I see this in terms of the ability to make connections. When I am standing up in front of a group of researchers doing a social media training, I am making pop-culture references, alluding to literary works, quoting song lyrics. When you get it right, you can see someone’s eyes light up. It’s just another way to connect – people sit up and pay attention if you can make a meaningful reference to the artist they love or the book they just read.

One of the questions we always use in our trainings is “so what?” So you are telling me about your science, but why should I care? Miles Davis has a famous song “So What?” and we play that in the background. It makes people smile. It makes it memorable. I love that. I really like this idea that we should be using the fullness of who we are and our creative selves, including all of the sensory modalities, to talk about the very abstract and difficult scientific topics we care about so much.

(DXS editor’s side note: A portion of the previous paragraph was delivered to me in song. What’s not to smile about?!?!)

DXS: How comfortable are you expressing your femininity and in what ways? How does this expression influence people’s perception of you in, say, a scientifically oriented context?

I feel very comfortable in my own skin, and who I am and where I come from does tend to be a classically feminine look (at least in terms of clothing choices and how I wear my hair). I am never quite certain the exact definition of “femininity”, but I don’t think how I look so much influences people’s perception of me as much as it opens up opportunities for us to discuss gender and personality and science.

Part of what I do for my work is to help scientists understand that in journalism, we need characters. So, I have the obligation to walk my talk – we are all the main characters in our own lives and we have to live with that and be true to that.

It brings up interesting questions of personality and privacy. I feel pretty comfortable talking about my clothes and my art and my dogs and my bread baking – but I also know that a lot of people don’t want that type of stuff out there. I like the challenge of helping them tell their own science stories and shine through as interesting people in a way that is authentic and represents who they are in a way that works for them.

DXS: Do you think that the combination of your non-science creativity and scientific-related activity shifts people’s perspectives or ideas about what a scientist or science communicator is? If you’re aware of such an influence, in what way, if any, do you use it to (for example) reach a different corner of your audience or present science in a different sort of way?

Sure, I think that I sometimes surprise people. For example, in the world of communications and journalism, we are seeing more and more that coding and programming has great value. To just look at me, you might not believe that I geek out over altmetrics and that I miss using MatLab.

It suprises people when they find this out, and I sort of like that. I know what it feels like to walk into a room and to be dismissed. I relish these opportunities because I consider them a challenge. Instead of feeling offended (though it can get tiring), my approach is thinking, “Guess what! I have something interesting to say, and you and I are actually going to connect, even though you don’t see it yet.”

I think that this sort of willingness to interact is something I try to help the scientists that I work with to understand. Maybe you think that you are going to be met with great opposition toward some subject like climate change, but if you have the willingness to approach it without assuming the worst, it opens new opportunties. I’m no Pollyanna, but I think relentless optimism and a commitment to finding common ground with others is very effective.

When I introduce social media to scientists, it has changed a lot over the last three years, but there is still a lot of skepticism and some outright scorn for “all those people online.” I like to encourage taking a step back from that in order to reveal all of the awesome things going on online and the ways you might engage. I truly enjoy the process of turning skeptics into something other than skeptics – I might not change them into believers, but they will at least be surprised and interested onlookers.

Liz Neeley’s Favorite Focaccia

INGREDIENTS:

Scant 4 cups white bread flour

1 tablespoon salt

Scant 1/2 cup olive oil

1 packet of active dry yeast

1 1/4 cups warm water

Favorite olives, roughly chopped if you prefer

Handful of fresh basil

TIME:

Start this mid-afternoon (between 3 and 4 hours before you want to eat it, depending on how fast you are in the kitchen)

RECIPE:

1.In a large bowl, combine the flour and salt with 1Ž4 cup of the olive oil, the yeast & the water. Mix with your hands for about 3 minutes.

Karyn Traphagen is the Executive Director of ScienceOnline Inc., a non-profit organization representing a diverse science community that cultivates conversations both online and face-to-face. At face-to-face events, including a perennially popular signature conference in North Carolina, ScienceOnline encourages creativity, collaborations, connections, and fun. Through social media, the ScienceOnline community listens, supports, shares, recommends, and reaches out. ScienceOnline also develops tools such as ScienceSeeker news river and curates The Open Lab, an annual anthology of the best science writing on the web.

Karyn previously taught physics at the high school, undergraduate and graduate levels. As a teacher, she sought to connect the science of the curriculum with the everyday life of her students and to instill lifelong skills for learning. Karyn completed graduate work at the University of Virginia and also studied at the University of Stellenbosch (South Africa). She has trained physics teachers through the University of Virginia’s Physics department and traveled to South Sudan to conduct professional development training for local teachers. She has more than 10 years of experience developing and teaching online courses.

In addition to her science work, Karyn maintains a freelance graphic design studio. Her latest project was a work on Ancient Near Eastern royal inscriptions.

Karyn lives in Durham, North Carolina, and she encourages readers wherever they are to Stay Curious at her blog. Connect with her on Twitter or Google+. You can also follow ScienceOnline on Twitter and Google+. [Editor's note: Karyn is also an official ADK46er, which is pretty incredible.]

DXS: First, can you give me a quick overview of what your scientific background is and your current connection to science?

Karyn enjoys creating art with…LEGOS!

I remember one of my favorite childhood gifts was a chemistry set and a microscope. My mother was a great role model. She left a job as a chemist to get married and raise a family, but she always instilled in me the attitude that if I was interested in any subject, I could learn it and do it. I always accepted a challenge.

Although I attended excellent public schools, I had to overcome some significant challenges. Our family was one of the only ones in our town designated as eligible for the new free lunch program, and I started high school when Title IX was passed (go ahead, do the math). This was an exciting time for girls in school–but not just for sports (our legacy to our 8thgrade class was a change in our public (!) school policy to allow girls to wear jeans).

I was thrilled to be the one of two females on our Math League squad and to have access to advanced science courses and labs in high school. It seems I always took a circuitous route though. I helped change the rules so that I could graduate in 3 years. I was very fortunate to have lots of opportunities after graduation (including being recruited for the first female class at West Point). But then, I took on other responsibilities and went back to school later to finish my degrees.

In addition to research, I have taught high school physics and physical science, undergrad physics (I especially liked the Physics for Non-Science majors!), and helped to develop a degree program in the university physics department for high school physics teachers. I’ve led sailing trips in the Bahamas for biology students and I’ve been trained by the American Meteorological Society to use live data in classrooms. I’ve even been a programmer. Obviously I’m interested in too many things for my own good.

Currently, I am the Executive Director of ScienceOnline, a non-profit organization that facilitates discussion about science through online networks and face-to-face events. We welcome all to the conversation – scientists, journalists, librarians, educators, students, and anyone interested in engaging in science. Four words that help to define ScienceOnline are: Connections, conversations, collaborations, and community. We also develop projects that work to connect scientists and their research to the public. I’m thrilled to be representing this thriving community, and I enjoy working with so many talented, brilliant, and fun people.

Karyn has traveled to South Sudan to conduct professional development training for local teachers.

DXS: What ways do you express yourself creatively that may not have a single thing to do with science?

I have an insatiable thirst to learn and try new things, which has resulted in a string of very diverse jobs. Over the years my creative activities (and jobs) have included medieval calligraphy, art, photography, mathematics (I count this as creative), LEGO creations, graphic design, garment creation, gardening, construction projects, violin/guitar (as musician and also instructor), studying ancient languages and writing systems (both real and created).

On the surface, many people think these are not “science-y” but really, they are all about science. Seeing that connection is something I love to introduce people to. My science career has included research that helps create more bio-fidelic crash test dummies (I worked with cadavers–this makes for great party stories), meteorology, high school physics teacher, and university physics instructor. I used to think that people would think I was flighty or unable to commit to a project. Now I see the benefits of having been successful at so many different skills and fields of study. The key was seeing how they all tapped into my curiosity and creativity.

DXS: Do you find that your scientific background informs your creativity, even though what you do may not specifically be scientific?

Definitely. Paying attention to the details of the world gives me opportunity to see beauty, symmetry, order, and chaos in unusual places. I am thrilled by the macro and the micro vision of our universe and lives (which is why I continue to study other fields of science in addition to physics). These are not only realms to explore with experiments, but to experience emotionally and to communicate creatively. I have learned to appreciate the details in science and that carries over into the art, photography, design, and construction projects that I may spend time on. Even my tattoo (snow crystals) reflects both beauty and science (and a lot of personal meaning too!)

DXS: Have you encountered situations in which your expression of yourself outside the bounds of science has led to people viewing you differently–either more positively or more negatively?

I think that sometimes the more conventional creative side of my life makes me seem more “human” and approachable. When non-science people ask what I do, I don’t usually start with “physics” in the answer because that often is hard for people to relate to and the conversation dies. But if they get to know some things I am interested in or the diversity of things I’ve created, and THEN learn about my science background, they are more likely to perceive me as more than a physics geek. At that point they feel more comfortable asking questions about science.

On the other hand, some of my science colleagues in the physics department saw those other activities as something that took me away from time that could be spent on physics. Even if they thought my non-science activities might be amazing they minimized their value. Thinking back now, maybe this is why I keep so much of what I do to myself and it takes time to draw out of me all the things that I have had the joy of learning and doing.

I think there is a geek aspect to many of the things I like to do. They don’t completely overlap with the same brand of geekiness though. It’s just that you align yourself with a community that is very engaged in a certain niche. A tribe if you will. Some of these tribes don’t understand each other very well, so I sometimes feel like an ambassador of the various communities I am a member of.

DXS: Have you found that your non-science expression of creativity/activity/etc. has in any way informed your understanding of science or how you may talk about it or present it to others?

Karyn collecting water samples in Molokai, Hawaii

Yes, I used to focus more on the narrow aspects of my field. Now I try to see interconnectedness—not only with other fields of science, but more broadly with day-to-day life. My “non-science” expressions are really gateways into understanding the science better or being willing to think more creatively about how to solve a research problem. Bottom line: I always want to stay curious. We don’t value curiosity enough. I think curiosity undergirds creativity. Curiosity doesn’t just beget science questions. We also have to ask, “What would happen if I mixed these colors together?” or “How small can I write with this pen nib and ink?” or “What kind of effects can I create in this photograph by changing the lens?”

DXS: How comfortable are you expressing your femininity and in what ways? How does this expression influence people’s perception of you in, say, a scientifically oriented context?

I really tried to think about this carefully. In the physics department at the university where I worked, my main concern was not the fact that I was in the minority (or that there were more men’s rooms in the building), but that the lab was freezing and I needed to keep warmer layers at work to survive! Basically, the lab protocols determined what kind of clothing and shoes I could wear, how I kept my hair (out of the way!) etc. I never felt those things were anything particularly against being feminine, but I didn’t go out of my way to wear makeup or dress special.

On the other hand, I do think that female visitors and students who dressed more feminine were definitely treated differently. I desperately wanted to be valued for my ideas and work ethic and not what I looked like or which bathroom I used, so I was probably more affected by others attitudes than I realize(d).

Probably the most feminine thing I’ve ever done was to have children and show my priority for them (I realize that there are fathers who do this too, so it may be more a parent thing than a feminine thing, but in the society I live in, it is still the mothers who bear the lion’s share of the responsibility for child-rearing). I had colleagues who could not understand some choices I made because of family. They felt I was wasting my potential (whatever that means!).

Now that I am not in a lab and don’t have small children at home, I alternate between tomboy and professional attire. I do like that it is easier to create a more feminine professional wardrobe these days.

I find it odd that women are complimented for their appearance more than men. I don’t think people realize how out-of-balance this is. I try to notice and mention men’s clothing and appearance as a small step toward equalizing that.

DXS: Do you think that the combination of your non-science creativity and scientific-related activity shifts people’s perspectives or ideas about what a scientist or science communicator is? If you’re aware of such an influence, in what way, if any, do you use it to (for example) reach a different corner of your audience or present science in a different sort of way?

I think that getting the attention of whatever audience you are addressing is paramount. You may have something wonderful to share, but if you don’t have their attention, it will fall to the ground. I want to develop a relationship with people in order to get them to trust me, believe me, and be interested in what I have to say. Dispensing information is not enough.

The manner in which I communicate makes all the difference in how the person will engage the topic. To do this, I need to listen first and understand who my audience is. Using creativity, I will then try to connect with each person or audience in a way that I hope will best bring them along the journey I have experienced. Some people will want to know more specific details, others will want to know how it affects their lives, and still others will challenge and question my thoughts and methods.

Using visual arts (e.g. fine arts, video, etc) can be as important as a data chart. As long as the conversation continues, then I have been successful in communicating. My goal is to make someone (whether a researcher or a teenager) so interested that they will take on a search for more information on their own. That’s really how we learn and retain best—to explore something we have invested our own time in.

I also use a variety of outlets for communication. There are definitely important and different roles for journals, conference presentations, Twitter, blogs, Google+, etc. These diverse outlets are just as important as creative ways of presenting material. Again, you must always be aware of your audience. I would use a museum’s Twitter account to communicate differently than I would my regular account.

DXS: If you had something you could say to the younger you about the role of expression and creativity in your chosen career path, what would you say?

Knowing myself, I’m not so sure that the younger me would listen to any advice I would give! In some ways, going through the experiences is what made me who I am and there are no short cuts for that. However, there are definitely things that would have been great to learn earlier on.

So, I would tell the younger me not to try to keep creative interests and career objectives separate or think that they have to be at odds with each other. They don’t need to be in competition for your attention. Creativity, job skills, life experiences, and responsibilities can interweave. You will not only be more content, but probably more productive in all your endeavors.

I would also tell her that “no” is not a dirty word and that it is ok to be selective in how you spend your time.

Our next installment of notable women in science brings us to chemists. Many of these women were born in the early part of the 20thcentury and forged their paths in tough times. All are still inspiring others today. Presented in no particular order:

Catherine Clarke Fenselau is a pioneer in mass spectrometry. Born in 1939, her interested in science was apparent before her 10th grade. She was encouraged to attend a women’s college, which at the time gave what she called “a special opportunity for serious-minded young women.” She graduated from Bryn Mawr with her A.B. in chemistry in 1961. Her graduate work at Stanford introduced her to the technology she would become known for, receiving her Ph.D. in analytical chemistry in 1965. Dr. Fenselau and her husband took positions at the Johns Hopkins University Medical School, at which time she had two sons. Johns Hopkins was under a mandate to accept female students and have female faculty at the time. Dr. Fenselau was made aware of the disparity of the treatment of male and female faculty, when in the 1970s the equal opportunity laws came into effect and she received an unexplained 25% raise. Her research resided in mass spectrometry, specifically in its use in biology. She became known as an anti-cancer researcher. Dr. Fenselau spoke often to chemists about feminism and goals, such as equal pay, opening closed career opportunities to women, and achieving the bonuses often only awarded to men. She has worked as an editor on several scientific journals. Some of her awards include the Garvan Medal, Maryland Chemist Award, and NIH Merit Award. Having proper help at work and at home, and having supportive mentors and spouse has helped her achieve her success.

Elizabeth Amy Kreiser Weisburger is considered a real-lifemedical sleuth. Born in 1924, Dr. Weisburger was one of 10 children and schooled at home for her early education. She received her B.S. in chemistry, cum laude, Phi Alpha Epsilon from Lebanon Valley College. She received her Ph.D. in organic chemistry in 1947 from the University of Cincinnati. She married and had three children. Her research has caused her to be proclaimed a pioneer in the field of chemical carcinogenesis. She balanced her busy life of working at the NCI, committee work, giving lectures, attending meetings, writing and reviewing papers while caring for children with the aid of housekeepers and nursery childcare. Some of her awards include the Garvan Medal and the HillebrandPrize. Her life philosophy is summed up with “Don’t take life so seriously; you’ll never get out of it alive.”

Helen M. Free is a major contributor to science and science education. Born in 1923, Ms. Free attended the College of Wooster, graduating with honors and a B.S. in 1944. In 1978, she earned a M.A. from Central Michigan University. In the meantime, she worked as a chemist at Miles Laboratories. She developed clinical effective and easy to use laboratory tests. She worked her way up through the company and also held an adjunct professor position at Indiana University, South Bend. Ms. Free has used her time to be active in professional societies and has served as president for the American Association for Clinical Chemistry and the American Chemical Society. Her awards include the Garvan Medal, a Distinguished Alumni Award from Wooster, and is the first recipient ofthe Public Outreach Award bearing her name.

Jeanette Grasselli Brown is an industry researcher and director. Born in 1929, she graduated summa cum laudewith her B.S. from Ohio University in 1950 and received her M.S. in 1958 from Western Reserve University. She worked at Standard Oil of Ohio (now BP of America), and became the first woman director of corporate research there. She has received numerous awards including the Garvan Medal, Ohio Women’s Hall of Fame, and the Fisher Award in Analytical Chemistry. She has published 75 papers in scientific journals, written 9 books, and received 7 honorary Doctorate of Science degrees. She is an activist for the future of women in science.

Jean’ne Marie Shreeve is an important fluorine chemist. Born in 1933, she encountered sexism through her mother’s inability to be employed despite her training as a schoolteacher. Dr. Shreeve graduated with a B.A. from Montana State University in 1953, followed by an M.S. in 1956 from the University of Minnesota, and a Ph.D. in inorganic chemistry in 1961 from the University of Washington. After graduating, she worked her way through the professorial ranks at the University of Idaho. Besides her own research, Dr. Shreeve has devoted herself to educating other chemists. Some of her awards include U.S. Ramsey Fellow, Alfred P. Sloan Fellow, and Garvan Medal.

Joyce Jacobson Kaufman is distinguished in many fields. Born in 1929, she was reading before the age of 2 and was a voracious reader as a child. This led to her reading the biography of Marie Curie, which inspired her to be a chemist. Dr. Kaufman received her B.S., M.A., and Ph.D. in physical chemistry from Johns Hopkins University in 1949, 1959, and 1960, respectively. She married and had a daughter. Her research in the application of quantum mechanics to chemistry, biology, and medicine led to her renown in several fields. She has also spent much time in service positions. Her awards include the Martin Company Gold Medal for Outstanding Scientific Accomplishments (received 3 times), the Garvan Medal, and honored as one of ten Outstanding Women in the State of Maryland.

Madeleine M. Joullie is known for elegant research and inspirational teaching. Born in 1927, her early life in Brazil was overly-protective, so her father encouraged her to attend school in the U.S.A. She received her B.Sc. from Simmons College in 1949, and her M.Sc. and Ph.D. in chemistry in 1950 and 1953, respectively, from the University of Pennsylvania. She then worked her way through the professorial ranks at the University of Pennsylvania. Initially, only the women graduate students would work with her, and they were few and far between. She has explored many research avenues over the course of her career. Her awards include the Garvan Medal, the American Cyanamid Faculty Award, the Henry HillAward, and the Lindback Award for Distinguished Teaching.

Marjorie Caserio is a researcher, educator, author, andacademic administrator. Born in 1929, she entered university with the goal of becoming a podiatrist in order to generic income. She received several rejections from colleges due to her gender, and eventually was accepted to be the only woman in her class. She received her B.S. from Chelsea College, University of London in 1950 and an M.A. and Ph.D from Bryn Mawr in 1951 and 1956. Dr. Caserio is co-author of one of the most popular organic chemistry textbooks in the chemistry during the 1960s and 1970s. Her awards include the Garvan Medal and John S. Guggenheim Foundation Fellow.

Mary Lowe Good has won several awards and is a public servant. Born in 1931, she was supported in her aspirations by her parents. She received her B.S. in 1950 from the University of Central Arkansas, which was then the Arkansas State Teachers College. She went on to receive her M.S. and Ph.D. in inorganic and radiochemistry from the University of Arkansas in 1953 and 1955. Her career began in academic, but an appointment to the National Science Foundation by President Carter changed the course of her career. She served the International Union of Pure and Applied Chemistry, and president of the American Chemical Society and Zonta International Foundation. Some of her awards include Garvan Medal, CharlesLathrop Parsons Award, and 18 honorary doctorates.

Ruth Mary Roan Benerito is an academic and government scientist. Born in 1916, she began college at the age of 15 at Sophie Newcomb College, the women’s college of Tulane and received her B.S. in 1935. She received her M.S. from Tulane University in 1938, which she worked half-time while working another job at the same time. She taught at Tulane and its colleges before going to the University of Chicago to get her Ph.D. in 1948 in physical chemistry, again working on a part-time basis. Her career oscillated between academia and industry, earning her a large number of awards, including the Federal Women’s Award, the Southern Chemist Award, and inducted as a Fellow into the American Institute of Chemists and Iota Sigma Pi.

Awards

The Garvan Medal is an award from the American Chemical Society to recognize distinguished service to chemistry by women chemists.

The Maryland Chemist Award recognizes and honors its members for outstanding achievement in the fields of chemistry.

The NIH Merit Award is asymbol of scientific achievement in the research community.

The Hillebrand Prize is awarded for original contributions to the science of chemistry.

The Distinguished Alumni Award from Woosteris presented annually to alumni who have distinguished themselves in one of more of the following area: professional career; service to humanity; and service to Wooster.

The American Institute of Chemistsadvances the chemical sciences by establishing high professional standards of practice and to emphasize the professional, ethical, economic, and social status of its members for the benefit of society as a whole.

Food engineering has been on an incredibly strange journey, but there is none stranger (at least to me) than the concept of in vitro meat. Colloquially referred to as “shmeat,” a term born out of mashing up the phrase “sheets of meat,” in vitro meat may be available in our grocer’s refrigerator section in just a few years. But how exactly is shmeat produced and how does it compare to, you know, that which is derived from actual animals? Here, I hope to shed some light on this petri dish to kitchen dish phenomenon.

The shmeaty deets

When it comes to producing shmeat, scientists are taking advantage the extensive cell culture technologies that have been developed over the course of the 20th century (for a brief history of these developments, check this out). Because of what we have learned, we can easily determine the conditions under which cells grow best, and swiftly turn a few cells into a few million cells. However, things can get a little tricky when growing complex, three-dimensional tissues like steak or boneless chicken breast.

For instance, lets consider a living, breathing cow. Most people seem to enjoy fancy cuts like beef tenderloin, which, before the butcher gets to it, is located near the back of the cow. In order for that meat to be nice and juicy, it needs to have enough nutrients and oxygen to grow. In addition, muscles (in this case, the tenderloin) need stimulation, and in the cow (and us too!) that is achieved by flexing and relaxing.

If shmeat is to be successfully engineered, scientists need to replicate all of the complexities that occur during the normal life of an actual animal. While the technology for making shmeat is still being optimized, the components involved in this meat-making scheme successfully address many of the major issues with growing whole tissues in a laboratory.

The first step in culturing meat is to get some muscle cells from an animal. Because cells divide as they grow, a single animal could, in theory, provide enough cells to make meat for many, many people – and for a long period of time. However, the major hurdle is creating a three-dimensional tissue, you know, something that would actually resemble a steak.

Normally, cells will grow in a single layer on a petri dish, with a thickness that can only be measured by using a microscope. Obviously that serving size would not be very satisfying. In order to create that delicious three-dimensional look, feel, and taste, and be substantial enough to count as a meal, scientists have developed a way to grow the muscle cells on scaffold made of natural and edible material. As sheets of cells grow on these scaffolds, they are laid on top of each other to bulk up the shmeat (hence “sheets of meat”). But, in order for the cells on the inside of this 3D mass to grow as well as the cells on the outside, there has to be an sufficient way to deliver nutrients and oxygen to all cells.

Back to the tenderloin – when it is still in the cow, the cells that make up this piece of meat are in close contact to a series of veins, arteries, and capillaries. Termed vasculature, this system allows for the cells to obtain nutrients and oxygen, while simultaneously allowing cells to dump any waste into the blood stream. There are some suggestionsthat the shmeat can be vascularized (grown such that a network of blood vessels are formed); however, the nutrient delivery system most widely used at this point is something called a bioreactor.

This contraption is designed to support biologically active materials and how it works is actually quite cool. The cells are placed in the cylindrical bioreactor, which spins at a rate that balances multiple physical forces, which keep the entire cell mass fully submerged in liquid growth medium at all times. This growth medium is constantly refreshed, ensuring that the cells are always supplied with a maximum level of growth factors. In essence, the shmeat is kept in a perpetual free fall state while it grows.

But there is one last piece to the meat-growing puzzle, and that is regular exercise. If we look at meat on a purely biological level, we would see that it is just a series of cells arranged to form muscle tissue. Without regular stimulation, muscles will waste away (atrophy). Clearly, wasting shmeat would not be very efficient (or tasty). So, shmeat engineers have reduced the basic biological process involved with muscle stimulationto the most basic components – mechanical contraction and electrical stimulation. Though mechanical contraction (the controlled stretching and relaxing of the growing muscle fibers) has been shown to be effective, it is not exactly feasible on a large scale. Electrical stimulation – the process of administering regular electrical pulses to the cells – is actually more effective than mechanical contraction and can be widely performed. Therefore, it seems to be a more viable option for shmeat production.

Why in the world would we grow meat in a petri dish?

Grill it, braise it, broil it, roast it – as long as it tastes good, most people don’t usually question the origins of their meat. Doing so could easily make one think twice about what they are eating. Traditionally speaking, every slab of meat begins with a live animal – cow, pig, lamb, poultry (yes, despite what my grandmother says, this vegetarian does consider chicken to be meat) – with each animal only being able to provide a finite number of servings. While shmeat does ultimately begin with a live animal, only a few muscle, fat, and other cells are required.

Given the theoretical amount that can be produced with just a few cells, the efficiency of traditional meat-generating farms and slaughterhouses is becoming increasingly scrutinized. There are obvious costs – economic, agricultural, environmental – that are associated with livestock, and it has been proposed(article behind dumb pay wall, grrrr….) that shmeat engineering would substantially cut these costs. For instance, it has been projected that shmeat production could use up to 45% less energy, compared to traditional farming methods. Furthermore, relative to the current meat production process, culturing shmeat would use 99% less land, 82-96% less water, and would significantly reduce the amount of greenhouse gasesproduced.

But the potential benefits of making the shift toward shmeat (as opposed to meat) doesn’t stop with its positive environmental impact. From a nutritional standpoint, it is possible to produce shmeat in a way that would significantly reduce the amount of saturated fat it contains. Additionally, there are technologies that would allow shmeat to be enriched with heart-healthy omega-3 fats, as well as other types of polyunsaturated fats. In essence, shmeat could possibly help combat our growing obesity epidemic, as well as the associated illnesses such as diabetes and heart disease. That’s *if* it can be produced in a way that is both affordable and widely available (more on that in a bit).

In terms of health, switching to shmeat would improve more than our waistlines. Because shmeat would be produced in a sterile environment, the incidence of E. coli and other bacterial and/or viral contamination would be next to nothing relative to current meat production methods. On a more superficial level, shmeat technology would allow for the introduction of some very exotic meats into the mainstream. Because this technology does not require an animal to be slaughtered (another good reason that supports shmeat productions) and it is not limited to the more common sources of meat, it would be entirely possible to make things like panda sausage and crocodile burgers. But, of course, getting people to actually eat meat grown in a test-tube is another issue…

The limitations of shmeat

Now that I’ve just spent a few paragraphs singing shmeat’s praises, it is probably best that I fill you in on some of the major roadblocks associated with shmeat production. According to scientists, there are two main concerns: the first is that shmeat production will not be subjected to the normal regulatory (homeostatic) mechanisms that naturally occur in animals (scientists are having trouble figuring out how to replicate these processes); and the second is that shmeat engineering technology has not evolved enough so that it can occur on an industrial scale. Because of these issues and others, the cost of culturing shmeat in the laboratory is very high. But, there has always got to be a starting point. As the technologies advance, the cost-production ratios will decrease and, eventually, shmeat will find its way to the dining table – our dining table.

Interestingly, the folks at PETA are all for shmeat and offered a one million dollar prize to the first group who could come up with the technology to make shmeat commercially available by June, 2012. Obviously, that did not happen, and the contest has been extended to January 2013 (this offer has been on the table since 2008). But, the first tastes test for shmeat hamburgers is going down in October of this year.

At the moment, the largest piece of shmeat to be created is about the size of a contact lens and my guess is that, barring unforeseen technological breakthroughs, this reward will go unclaimed for a long, long time. But, many a miracle has been known to happen in about nine months time…

A few final thoughts on shmeat

With the world population expected to hit 9 billion by 2050, which will be accompanied by a major increase in the need for the amount of food produced, perhaps shmeat technology will become one of the critical innovations required for our collective survival on this planet. But, there is just one thing: the ick factor. It is a little hard for me to weigh in on this issue because almost all meat seems gross to me (unless it is a pulled pork sandwich, lovingly made by my long-time pal and professional chef – Julie Hall). While most of my peers have less of an aversion to meat, I can’t imagine that they would eagerly line up for a whopping serving of lab-grown shmeat.

But, say scientists finally figure it out and shmeat production is scaled up for mass consumption – how will the agricultural sector react? As of right now, the agricultural industry in the USA is worth over $70 billion, with a yearly beef consumptiontipping over the 26 million pound mark (of which 8.7% is exported). Shmeat probably has definitely gotten the attention of cattle farmers (and other meat farmers/production companies) and, given the size of this industry, I wonder how much muscle will be used to block shmeat from becoming a household phenomenon.

Over all, I think that shmeat is a revolutionary idea as it could have a significant impact on humanity. However, there are many complex questions that need to be both asked andanswered. As excited as I am at the thought of not having to kill an animal to eat a steak, I still remain skeptical (though this sentiment may not have been fully present for the majority of this post). Will shmeat be produced in such a way that it will be indistinguishable from traditional meat? Additionally, will shmeat live up to all of these expectations? I am going to try and keep a positive outlook with this one. Perhaps the next time I actually step foot in a kitchen to prepare a meal, I’ll follow Randy’s lead by making a shmeatloaf, served alongside a heaping side of mashed potatoes. Now that’s some pretty cool kitchen science.

And now, an oldie but a goodie (let it be known that I am in love with Stephen Colbert):

The following was originally posted over at The Mother Geek (RIP) in January of this year. The guest author is Alice Callahan, who is a research scientist turned stay-at-home mom. She lives in Eugene, Oregon, with her husband and 14-month-old daughter. Alice writes about the science of parenting, as well as her adventures in mothering, at scienceofmom.com. You can also find Alice on Twitter.

Via Creative Commons

Having a PhD in science makes my job as a mother easier – but maybe not in the ways that you might expect.

My PhD is in Nutrition, so you would think that getting my kid to eat well would come easy for me. Unfortunately, that has not been the case. I’ve logged more than two years of postdoc research on fetal programming – how the uterine environment affects outcomes in babies. You might think that this helped me to do everything right during my pregnancy. Instead, I think it just led to more worry about all of the ways I might be damaging my unborn child. Stress! Sugar! BPA! Lab chemical exposure! OMG! More stress!

Sure, I have more knowledge than the average mother. Sometimes that is helpful. And sometimes it is not. And knowing how to do a literature search to try to answer my parenting questions often leads to further sleep deprivation as I slog through Pubmed hits and come out on the other side with more confusion. Sometimes my drive to find scientific answers for my parenting questions just distracts me from my instinct – not that my maternal instinct is all that amazing, but I do know my baby better than anyone else in the world.

So how does being a scientist make parenting easier for me? As a scientist mother, I trust other scientists. And I trust doctors. I even trust government agencies, which bring together the best scientists and doctors in a field to review the research and make recommendations for the good of public health.

I trust scientists and doctors, because I have worked side-by-side with them for a decade, andI know that they are not only knowledgeable,but by and large, they are overwhelmingly good people. At some point, you have to trust someone.

I trust scientists and doctors.

I trust scientists, because I know that the vast majority of them are just underpaid nerds who are really passionate about what they do. They are driven by the desire to find the truth about a question and they work, day in and day out, in that pursuit. In addition, I know that scientists don’t always agree, so when there is a general consensus among the majority of scientists about something, such as vaccine safety or global warming, I feel confident in that conclusion.

Contrary to many claims on the Internet, scientists are not in bed with Big Pharma, conspiring make millions at the expense of your child’s health. They are in bed with their husbands and wives, probably chatting about their latest failed cell culture experiment.

I also trust science because I understand the peer review process all too well. Although it has its flaws and as maddening as it is when I am the one being reviewed, I have confidence that the peer review process is highly effective at weeding out the kooks and pseudoscientists and the conflicts of interest. (Unfortunately, there are a few kooky psuedoscientists out there with serious conflicts of interest, and it just so happens that one of them managed to publish fraudulent research linking the MMR vaccine and autism. Many studies have since shown that such a link does not exist, but it took 12 years for Andrew Wakefield’s Lancet paper to be retracted. How many dollars have been spent and how many people made sick or worse in the continuing fallout and confusion about this public health scare? When the peer review system fails, it can be truly devastating.)

I trust doctors because I know that most of them are, first and foremost, humanitarians at heart, especially those that have chosen to work in primary care. I know how hard doctors work to become competent in the vast ocean of information about pathologies of the human body. I know how seriously they take their responsibility of our health.

I especially trust pediatricians. They have chosen one of the lowest-paid specialties simply because they love working with kids. I know that every pediatrician, at some point during her training or career, has likely cared for a child who was dying of a disease that could have been prevented by vaccination, and that memory haunts her as she faces parents afraid of vaccinating their children. Doctors are not conspiring against us. They want to help us make the best choices for our children, more than anything in the world.

Because I trust scientists and doctors, I didn’t question the CDC’s vaccination schedule. I didn’t pore over vaccine research or agonize about the decision to vaccinate my child. Instead, I trusted that the committees of experts at the CDC and AAP carefully make the best recommendations possible based on the data available.

Maybe that is naïve. Maybe I am a lazy mother for not trying to become a vaccine expert before I allowed those first needles to enter my daughter’s thigh. Maybe. But I also think it would be naïve for me to think that I could become an expert on vaccinations, that I could know and understand the field better than the committees of scientists and doctors who have made this their life’s work.

I know how much work it took me to become an expert on one or two corners of nutrition and fetal physiology. It took thousands of hours of reading textbooks and journal articles, sitting in lectures, attending conferences, and struggling at the lab bench before I started to feel even a little bit comfortable calling myself an expert in any field. So I think it is naïve for a parent to think that she can become an expert on vaccines by spending some time on the Internet, reading questionable sources, almost all of which have some agenda. I accept that I can’t know everything, and I have enough faith in humanity that I trust others who know more than me.

It is not that I don’t question scientists and doctors. I do. For example, I recognize that government agencies and medical organizations often have a lag time for adopting the latest science into their recommendations. I recognize that tradition, culture, politics, and economics all influence those recommendations, and they are not without fault.

I certainly question my doctors, because I know they are each fallible human beings, and they can’t know everything. I brought a stack of journal articles to my OB to convince her to delay cord clamping at my delivery. I did so much research on infant iron nutrition and came to my daughter’s 9-month checkup with so many questions that my pediatrician looked me in the eye and said, “You’re worried enough for both of us about BabyC’s iron.” Although I question my doctors, I also trust that they are adept at discerning fake science from real science. If I bring my doctor the sources I am using to inform my questions or concerns, she should be able to judge whether or not they are trustworthy and have a real discussion with me about factors that I may not have considered.

In truth, I do follow the vaccine debate closely, but not because I wonder if I am doing the right thing by vaccinating my child. I follow the vaccine debate out of interest for how misinformation can explode in a way that creates a public health crisis. I find myself increasingly concerned about the low rate of vaccination in my own community. I worry for the newborns in our town who have not yet had a chance to be vaccinated and for the individuals who cannot be vaccinated due to health conditions. I am starting to feel like I have a responsibility to share accurate information with mothers and fathers struggling with the decision of whether or not to vaccinate, because misinformation is doing real harm.

It is good to question our parenting decisions and in doing so, become more educated about them. However, as a scientist, I’m happy to defer to other scientists about some of the biggest parenting decisions I have faced. I am grateful for their decades of research forming the foundation of our understanding of child health and for the good-hearted doctors who care for my family. They have made my job as a mother a lot easier. I can spend less time worrying and more time playing with my daughter and soaking up the time with her as she grows up way too fast.

Thanks, science, for making it easier to be a mom.

These views are the opinion of the author and do not necessarily reflect or disagree with those of the DXS editorial team.